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2b6p

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[[Image:2b6p.gif|left|200px]]
 
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{{Structure
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==X-ray structure of lens Aquaporin-0 (AQP0) (lens MIP) in an open pore state==
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|PDB= 2b6p |SIZE=350|CAPTION= <scene name='initialview01'>2b6p</scene>, resolution 2.40&Aring;
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<StructureSection load='2b6p' size='340' side='right'caption='[[2b6p]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2b6p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B6P FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b6p OCA], [https://pdbe.org/2b6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b6p RCSB], [https://www.ebi.ac.uk/pdbsum/2b6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b6p ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1sor|1SOR]], [[2b6o|2B6O]], [[1ymg|1YMG]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b6p OCA], [http://www.ebi.ac.uk/pdbsum/2b6p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b6p RCSB]</span>
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[https://www.uniprot.org/uniprot/MIP_BOVIN MIP_BOVIN] Water channel. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core.<ref>PMID:16319884</ref>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b6/2b6p_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b6p ConSurf].
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<div style="clear:both"></div>
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'''X-ray structure of lens Aquaporin-0 (AQP0) (lens MIP) in an open pore state'''
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==See Also==
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*[[Aquaporin 3D structures|Aquaporin 3D structures]]
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== References ==
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==Overview==
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<references/>
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Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and forms the thin junctions between fibre cells. Here we describe a 1.9 A resolution structure of junctional AQP0, determined by electron crystallography of double-layered two-dimensional crystals. Comparison of junctional and non-junctional AQP0 structures shows that junction formation depends on a conformational switch in an extracellular loop, which may result from cleavage of the cytoplasmic amino and carboxy termini. In the centre of the water pathway, the closed pore in junctional AQP0 retains only three water molecules, which are too widely spaced to form hydrogen bonds with each other. Packing interactions between AQP0 tetramers in the crystalline array are mediated by lipid molecules, which assume preferred conformations. We were therefore able to build an atomic model for the lipid bilayer surrounding the AQP0 tetramers, and we describe lipid-protein interactions.
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__TOC__
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</StructureSection>
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==About this Structure==
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2B6P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B6P OCA].
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==Reference==
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Lipid-protein interactions in double-layered two-dimensional AQP0 crystals., Gonen T, Cheng Y, Sliz P, Hiroaki Y, Fujiyoshi Y, Harrison SC, Walz T, Nature. 2005 Dec 1;438(7068):633-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16319884 16319884]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cheng, Y.]]
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[[Category: Cheng Y]]
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[[Category: Fujiyoshi, Y.]]
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[[Category: Fujiyoshi Y]]
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[[Category: Gonen, T.]]
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[[Category: Gonen T]]
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[[Category: Harrison, S C.]]
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[[Category: Harrison SC]]
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[[Category: Hiroaki, Y.]]
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[[Category: Hiroaki Y]]
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[[Category: Sliz, P.]]
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[[Category: Sliz P]]
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[[Category: Walz, T.]]
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[[Category: Walz T]]
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[[Category: aqp0]]
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[[Category: aquaporin]]
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[[Category: aquaporin-0]]
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[[Category: lens mip]]
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[[Category: membrane protein;]]
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[[Category: open water pore]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:02:15 2008''
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Current revision

X-ray structure of lens Aquaporin-0 (AQP0) (lens MIP) in an open pore state

PDB ID 2b6p

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